Current Applications of Bicelles in NMR Studies of Membrane-Associated Amphiphiles and Proteins

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• 作者：R. Scott Prosser ; Ferenc Evanics ; Julianne L. Kitevski ; and M. Sameer Al-Abdul-Wahid
• 刊名：Biochemistry
• 出版年：2006
• 出版时间：July 18, 2006
• 年：2006
• 卷：45
• 期：28
• 页码：8453 - 8465
• 全文大小：430K
• 年卷期：v.45,no.28(July 18, 2006)
• ISSN：1520-4995

文摘

This review covers current trends in studies of membrane amphiphiles and membrane proteinsusing both fast tumbling bicelles and magnetically aligned bicelle media for both solution state and solidstate NMR. The fast tumbling bicelles provide a versatile biologically mimetic membrane model, whichin many cases is preferable to micelles, both because of the range of lipids and amphiphiles that may becombined and because radius of curvature effects and strain effects common with micelles may be avoided.Drug and small molecule binding and partitioning studies should benefit from their application in fasttumbling bicelles, tailored to mimic specific membranes. A wide range of topology and immersion depthstudies have been shown to be effective in fast tumbling bicelles, while residual dipolar couplings addanother dimension to structure refinement possibilities, particularly for situations in which the peptide isuniformly labeled with ¹⁵N and ¹³C. Solid state NMR studies of polytopic transmembrane proteinsdemonstrate that it is possible to express, purify, and reconstitute membrane proteins, ranging in sizefrom single transmembrane domains to seven-transmembrane GPCRs, into bicelles. The line widths andquality of the resulting ¹⁵NH dipole-¹⁵N chemical shift spectra demonstrate that there are no insurmountableobstacles to the study of large membrane proteins in magnetically aligned media.